ATP fosters the tuning of nanostructured CeO peroxidase-like activity for promising antibacterial performance
An enduring and formidable challenge in nanozyme catalysis is low sensitivity and operational instability, which impedes their biological usage. In this contribution fluorite-structured cerium oxide nanocrystals (CeO 2 NCs) with ∼23.04% Ce 3+ fraction were found to possess recyclable (10 cycles) per...
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creator | Chishti, Benazir Fouad, H Seo, H. K Alothman, Othman Y Ansari, Z. A Ansari, S. G |
description | An enduring and formidable challenge in nanozyme catalysis is low sensitivity and operational instability, which impedes their biological usage. In this contribution fluorite-structured cerium oxide nanocrystals (CeO
2
NCs) with ∼23.04% Ce
3+
fraction were found to possess recyclable (10 cycles) peroxidase (POD)-like activity capable of catalyzing the oxidation of 3,3′,5,5′-tetramethylbenzidine (TMB) when hydrogen peroxide (H
2
O
2
) serves as oxidant, and exhibit high substrate affinity under acidic conditions. We tuned this catalytic activity at neutral pH (7.4) using adenosine triphosphate (ATP). It was found that ATP stabilizes the oxidation product and improves catalytic performance at neutral pH. Mechanistic investigation reveals that oxidation of TMB originates from catalyst (CeO
2
NCs)-directed decomposition of H
2
O
2
, which pools hydroxyl (&z.rad;OH) radicals under acidic and neutral environments; kinetic studies indicate a Michaelis-Menten enzyme kinetic model. Notably, above pH 4.5, ATP facilitates a drop in catalyst
K
m
values of about 2.5 and 4.79 times for TMB and H
2
O
2
, respectively, suggesting high affinity favouring reaction feasibility at neutral pH. Screening of other relevant modulators shows the following order in promoting catalysis at neutral pH: ATP > histidine ≥ ADP >AMP. This pH-tunable POD-mimic CeO
2
nanozyme realizes a nanocatalytic strategy for sourcing &z.rad;OH radicals, which contributes to anti-bacterial performance. This study provides new insight for designing nanozymes and expanding the use of nanozymes in biomedicine.
Recyclable nano CeO
2
POD mimic records a
K
m
reduction (∼30% and ∼19.72% for TMB and H
2
O
2
, respectively) in 900 seconds at pH 4.5. ATP boosts catalytic feasibility in nano CeO
2
at physiological pH. |
doi_str_mv | 10.1039/c9nj05955e |
format | Article |
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2
NCs) with ∼23.04% Ce
3+
fraction were found to possess recyclable (10 cycles) peroxidase (POD)-like activity capable of catalyzing the oxidation of 3,3′,5,5′-tetramethylbenzidine (TMB) when hydrogen peroxide (H
2
O
2
) serves as oxidant, and exhibit high substrate affinity under acidic conditions. We tuned this catalytic activity at neutral pH (7.4) using adenosine triphosphate (ATP). It was found that ATP stabilizes the oxidation product and improves catalytic performance at neutral pH. Mechanistic investigation reveals that oxidation of TMB originates from catalyst (CeO
2
NCs)-directed decomposition of H
2
O
2
, which pools hydroxyl (&z.rad;OH) radicals under acidic and neutral environments; kinetic studies indicate a Michaelis-Menten enzyme kinetic model. Notably, above pH 4.5, ATP facilitates a drop in catalyst
K
m
values of about 2.5 and 4.79 times for TMB and H
2
O
2
, respectively, suggesting high affinity favouring reaction feasibility at neutral pH. Screening of other relevant modulators shows the following order in promoting catalysis at neutral pH: ATP > histidine ≥ ADP >AMP. This pH-tunable POD-mimic CeO
2
nanozyme realizes a nanocatalytic strategy for sourcing &z.rad;OH radicals, which contributes to anti-bacterial performance. This study provides new insight for designing nanozymes and expanding the use of nanozymes in biomedicine.
Recyclable nano CeO
2
POD mimic records a
K
m
reduction (∼30% and ∼19.72% for TMB and H
2
O
2
, respectively) in 900 seconds at pH 4.5. ATP boosts catalytic feasibility in nano CeO
2
at physiological pH.</description><identifier>ISSN: 1144-0546</identifier><identifier>EISSN: 1369-9261</identifier><identifier>DOI: 10.1039/c9nj05955e</identifier><language>eng</language><ispartof>New journal of chemistry, 2020-07, Vol.44 (26), p.11291-1133</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Chishti, Benazir</creatorcontrib><creatorcontrib>Fouad, H</creatorcontrib><creatorcontrib>Seo, H. K</creatorcontrib><creatorcontrib>Alothman, Othman Y</creatorcontrib><creatorcontrib>Ansari, Z. A</creatorcontrib><creatorcontrib>Ansari, S. G</creatorcontrib><title>ATP fosters the tuning of nanostructured CeO peroxidase-like activity for promising antibacterial performance</title><title>New journal of chemistry</title><description>An enduring and formidable challenge in nanozyme catalysis is low sensitivity and operational instability, which impedes their biological usage. In this contribution fluorite-structured cerium oxide nanocrystals (CeO
2
NCs) with ∼23.04% Ce
3+
fraction were found to possess recyclable (10 cycles) peroxidase (POD)-like activity capable of catalyzing the oxidation of 3,3′,5,5′-tetramethylbenzidine (TMB) when hydrogen peroxide (H
2
O
2
) serves as oxidant, and exhibit high substrate affinity under acidic conditions. We tuned this catalytic activity at neutral pH (7.4) using adenosine triphosphate (ATP). It was found that ATP stabilizes the oxidation product and improves catalytic performance at neutral pH. Mechanistic investigation reveals that oxidation of TMB originates from catalyst (CeO
2
NCs)-directed decomposition of H
2
O
2
, which pools hydroxyl (&z.rad;OH) radicals under acidic and neutral environments; kinetic studies indicate a Michaelis-Menten enzyme kinetic model. Notably, above pH 4.5, ATP facilitates a drop in catalyst
K
m
values of about 2.5 and 4.79 times for TMB and H
2
O
2
, respectively, suggesting high affinity favouring reaction feasibility at neutral pH. Screening of other relevant modulators shows the following order in promoting catalysis at neutral pH: ATP > histidine ≥ ADP >AMP. This pH-tunable POD-mimic CeO
2
nanozyme realizes a nanocatalytic strategy for sourcing &z.rad;OH radicals, which contributes to anti-bacterial performance. This study provides new insight for designing nanozymes and expanding the use of nanozymes in biomedicine.
Recyclable nano CeO
2
POD mimic records a
K
m
reduction (∼30% and ∼19.72% for TMB and H
2
O
2
, respectively) in 900 seconds at pH 4.5. ATP boosts catalytic feasibility in nano CeO
2
at physiological pH.</description><issn>1144-0546</issn><issn>1369-9261</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNp9UMtKxDAUDaLgOLpxL8QPqObVtFkOxRcMjIvuS5reasY2LUkqzt-bQcGdq3M5LzgXoWtK7ijh6t4otye5ynM4QSvKpcoUk_Q03VSIjORCnqOLEPaEUFpIukLjpn7F_RQi-IDjO-C4OOve8NRjp13i_WLi4qHDFezwDH76sp0OkA32A7A20X7aeEgNHs9-Gm04hrWLtk0aeKuHYyjJo3YGLtFZr4cAV7-4RvXjQ109Z9vd00u12Waech4z05aF5ILo0hSKMaoYEMOV5NKIoi17AabNRdrLaF8wANVqLvOS0VIzpVq-Rrc_tT6YZvZ21P7Q_L2mmbs-eW7-8_Bvmjpk6A</recordid><startdate>20200714</startdate><enddate>20200714</enddate><creator>Chishti, Benazir</creator><creator>Fouad, H</creator><creator>Seo, H. K</creator><creator>Alothman, Othman Y</creator><creator>Ansari, Z. A</creator><creator>Ansari, S. G</creator><scope/></search><sort><creationdate>20200714</creationdate><title>ATP fosters the tuning of nanostructured CeO peroxidase-like activity for promising antibacterial performance</title><author>Chishti, Benazir ; Fouad, H ; Seo, H. K ; Alothman, Othman Y ; Ansari, Z. A ; Ansari, S. G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-r133t-cb876340a8c7922192e0c39636c47b8f4ecb5403921f72ee9ba3658218a299b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chishti, Benazir</creatorcontrib><creatorcontrib>Fouad, H</creatorcontrib><creatorcontrib>Seo, H. K</creatorcontrib><creatorcontrib>Alothman, Othman Y</creatorcontrib><creatorcontrib>Ansari, Z. A</creatorcontrib><creatorcontrib>Ansari, S. G</creatorcontrib><jtitle>New journal of chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chishti, Benazir</au><au>Fouad, H</au><au>Seo, H. K</au><au>Alothman, Othman Y</au><au>Ansari, Z. A</au><au>Ansari, S. G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ATP fosters the tuning of nanostructured CeO peroxidase-like activity for promising antibacterial performance</atitle><jtitle>New journal of chemistry</jtitle><date>2020-07-14</date><risdate>2020</risdate><volume>44</volume><issue>26</issue><spage>11291</spage><epage>1133</epage><pages>11291-1133</pages><issn>1144-0546</issn><eissn>1369-9261</eissn><abstract>An enduring and formidable challenge in nanozyme catalysis is low sensitivity and operational instability, which impedes their biological usage. In this contribution fluorite-structured cerium oxide nanocrystals (CeO
2
NCs) with ∼23.04% Ce
3+
fraction were found to possess recyclable (10 cycles) peroxidase (POD)-like activity capable of catalyzing the oxidation of 3,3′,5,5′-tetramethylbenzidine (TMB) when hydrogen peroxide (H
2
O
2
) serves as oxidant, and exhibit high substrate affinity under acidic conditions. We tuned this catalytic activity at neutral pH (7.4) using adenosine triphosphate (ATP). It was found that ATP stabilizes the oxidation product and improves catalytic performance at neutral pH. Mechanistic investigation reveals that oxidation of TMB originates from catalyst (CeO
2
NCs)-directed decomposition of H
2
O
2
, which pools hydroxyl (&z.rad;OH) radicals under acidic and neutral environments; kinetic studies indicate a Michaelis-Menten enzyme kinetic model. Notably, above pH 4.5, ATP facilitates a drop in catalyst
K
m
values of about 2.5 and 4.79 times for TMB and H
2
O
2
, respectively, suggesting high affinity favouring reaction feasibility at neutral pH. Screening of other relevant modulators shows the following order in promoting catalysis at neutral pH: ATP > histidine ≥ ADP >AMP. This pH-tunable POD-mimic CeO
2
nanozyme realizes a nanocatalytic strategy for sourcing &z.rad;OH radicals, which contributes to anti-bacterial performance. This study provides new insight for designing nanozymes and expanding the use of nanozymes in biomedicine.
Recyclable nano CeO
2
POD mimic records a
K
m
reduction (∼30% and ∼19.72% for TMB and H
2
O
2
, respectively) in 900 seconds at pH 4.5. ATP boosts catalytic feasibility in nano CeO
2
at physiological pH.</abstract><doi>10.1039/c9nj05955e</doi><tpages>13</tpages></addata></record> |
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language | eng |
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source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
title | ATP fosters the tuning of nanostructured CeO peroxidase-like activity for promising antibacterial performance |
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